PTPRH

PTPRH

Protein tyrosine phosphatase, receptor type, H, also known as PTPRH, is a human gene.cite web | title = Entrez Gene: PTPRH protein tyrosine phosphatase, receptor type, H| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5794| accessdate = ]

PBB_Summary
section_title =
summary_text = The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and a single intracytoplasmic catalytic domain, and thus represents a receptor-type PTP. The extracellular region contains eight fibronectin type III-like repeats and multiple N-glycosylation sites. The gene was shown to be expressed primarily in brain and liver, and at a lower level in heart and stomach. It was also found to be expressed in several cancer cell lines, but not in the corresponding normal tissues.cite web | title = Entrez Gene: PTPRH protein tyrosine phosphatase, receptor type, H| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5794| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Matozaki T, Suzuki T, Uchida T, "et al." |title=Molecular cloning of a human transmembrane-type protein tyrosine phosphatase and its expression in gastrointestinal cancers. |journal=J. Biol. Chem. |volume=269 |issue= 3 |pages= 2075–81 |year= 1994 |pmid= 8294459 |doi=
*cite journal | author=Noguchi T, Tsuda M, Takeda H, "et al." |title=Inhibition of cell growth and spreading by stomach cancer-associated protein-tyrosine phosphatase-1 (SAP-1) through dephosphorylation of p130cas. |journal=J. Biol. Chem. |volume=276 |issue= 18 |pages= 15216–24 |year= 2001 |pmid= 11278335 |doi= 10.1074/jbc.M007208200
*cite journal | author=Marneros AG, Mehenni H, Reichenberger E, "et al." |title=Gene for the human transmembrane-type protein tyrosine phosphatase H (PTPRH): genomic structure, fine-mapping and its exclusion as a candidate for Peutz-Jeghers syndrome. |journal=Cytogenet. Cell Genet. |volume=92 |issue= 3-4 |pages= 213–6 |year= 2001 |pmid= 11435690 |doi=
*cite journal | author=Takada T, Noguchi T, Inagaki K, "et al." |title=Induction of apoptosis by stomach cancer-associated protein-tyrosine phosphatase-1. |journal=J. Biol. Chem. |volume=277 |issue= 37 |pages= 34359–66 |year= 2002 |pmid= 12101188 |doi= 10.1074/jbc.M206541200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Nagano H, Noguchi T, Inagaki K, "et al." |title=Downregulation of stomach cancer-associated protein tyrosine phosphatase-1 (SAP-1) in advanced human hepatocellular carcinoma. |journal=Oncogene |volume=22 |issue= 30 |pages= 4656–63 |year= 2003 |pmid= 12879010 |doi= 10.1038/sj.onc.1206588
*cite journal | author=Pasquali C, Curchod ML, Wälchli S, "et al." |title=Identification of protein tyrosine phosphatases with specificity for the ligand-activated growth hormone receptor. |journal=Mol. Endocrinol. |volume=17 |issue= 11 |pages= 2228–39 |year= 2004 |pmid= 12907755 |doi= 10.1210/me.2003-0011
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, "et al." |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Нужно сделать НИР?

Look at other dictionaries:

  • Guanylate cyclase — (EC 4.6.1.2, also known as guanylyl cyclase, guanyl cyclase or GC) is a lyase enzyme. Contents 1 Reaction 2 Types 3 Function …   Wikipedia

  • Protein tyrosine phosphatase — Protein tyrosine phosphatases (PTPs) are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins. Protein tyrosine (pTyr) phosphorylation is a common post translational modification that can create novel… …   Wikipedia

  • DUSP1 — Dual specificity phosphatase 1 Identifiers Symbols DUSP1; CL100; HVH1; MKP 1; MKP1; PTPN10 External IDs …   Wikipedia

  • NPR1 — Natriuretic peptide receptor A/guanylate cyclase A (atrionatriuretic peptide receptor A) Identifiers Symbols NPR1; ANPRA; ANPa; GUC2A; GUCY2A; NPRA External IDs …   Wikipedia

  • Myotubularin 1 — Identifiers Symbols MTM1; CNM; MTMX; XLMTM External IDs OMIM: …   Wikipedia

  • DUSP6 — Dual specificity phosphatase 6 PDB rendering based on 1hzm …   Wikipedia

  • DUSP3 — Dual specificity phosphatase 3 PDB rendering based on 1j4x …   Wikipedia

  • Myotubularin — related Structure of a phosphoinositide phosphatase.[1] Identifiers Symbol Myo …   Wikipedia

  • DUSP4 — Dual specificity phosphatase 4 Identifiers Symbols DUSP4; HVH2; MKP 2; MKP2; TYP External IDs …   Wikipedia

  • DUSP10 — Dual specificity phosphatase 10 PDB rendering based on 1zzw …   Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”